Regulation of Human Endothelial Cell Focal Adhesion Sites and Migration by cGMP-dependent Protein Kinase I*

@article{Smolenski2000RegulationOH,
  title={Regulation of Human Endothelial Cell Focal Adhesion Sites and Migration by cGMP-dependent Protein Kinase I*},
  author={A. Smolenski and W. Poller and U. Walter and S. Lohmann},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={25723 - 25732}
}
cGMP-dependent protein kinase type I (cGK I), a major constituent of the atrial natriuretic peptide (ANP)/nitric oxide/cGMP signal transduction pathway, phosphorylates the vasodilator-stimulated phosphoprotein (VASP), a member of the Ena/VASP family of proteins involved in regulation of the actin cytoskeleton. Here we demonstrate that stimulation of human umbilical vein endothelial cells (HUVECs) by both ANP and 8-(4-chlorophenylthio)guanosine 3′:5′-monophosphate (8-pCPT-cGMP) activates… Expand
Protein kinase G signaling disrupts Rac1-dependent focal adhesion assembly in liver specific pericytes.
Novel roles of cAMP/cGMP‐dependent signaling in platelets
  • A. Smolenski
  • Chemistry, Medicine
  • Journal of thrombosis and haemostasis : JTH
  • 2012
Thrombospondin-1 inhibits endothelial cell responses to nitric oxide in a cGMP-dependent manner.
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